TGase5 Inhibitors

TGase5 inhibitors represent compounds that, either directly or indirectly, can inhibit the enzymatic activity of TGase5. Given that TGase5 is a member of the transglutaminase family, many of these inhibitors draw their origins from the broader spectrum of transglutaminase inhibitors. The principal mode of inhibition for many of these compounds revolves around competition at the enzyme's active site. For example, Cystamine, Monodansylcadaverine, and Z-DON-Val-Pro-Leu-OMe can block or compete with the active site, reducing the enzyme's capability to catalyze protein crosslinking.

Certain inhibitors, such as Adenosine dialdehyde, target ancillary sites like the GTP-binding site. This inhibition mechanism can impact the enzyme's conformation or functionality, leading to its reduced activity. In the context of TGase5, which has been associated with epidermal differentiation, inhibiting its activity can influence processes like cornified envelope formation. Calcium chelators like BAPTA and EGTA serve as inhibitors by removing calcium ions from the enzyme's vicinity. Since some transglutaminase activities are calcium-dependent, sequestering calcium can effectively reduce enzyme function.